SHU1_SCHPO
ID SHU1_SCHPO Reviewed; 226 AA.
AC Q92340;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 25-MAY-2022, entry version 100.
DE RecName: Full=High affinity heme transporter {ECO:0000305};
DE Flags: Precursor;
GN Name=shu1 {ECO:0000303|PubMed:25733668};
GN ORFNames=SPAC1F8.02c {ECO:0000312|PomBase:SPAC1F8.02c};
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP FUNCTION, SUBCELLULAR LOCATION, INDUCTION, DISRUPTION PHENOTYPE, AND
RP MUTAGENESIS OF CYS-72; CYS-87; CYS-92 AND CYS-101.
RX PubMed=25733668; DOI=10.1074/jbc.m115.642058;
RA Mourer T., Jacques J.F., Brault A., Bisaillon M., Labbe S.;
RT "Shu1 is a cell-surface protein involved in iron acquisition from heme in
RT Schizosaccharomyces pombe.";
RL J. Biol. Chem. 290:10176-10190(2015).
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF
RP CYS-72; CYS-87; CYS-92 AND CYS-101.
RX PubMed=28193844; DOI=10.1074/jbc.m117.776807;
RA Mourer T., Normant V., Labbe S.;
RT "Heme Assimilation in Schizosaccharomyces pombe Requires Cell-surface-
RT anchored Protein Shu1 and Vacuolar Transporter Abc3.";
RL J. Biol. Chem. 292:4898-4912(2017).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=29549126; DOI=10.1074/jbc.ra118.002132;
RA Normant V., Mourer T., Labbe S.;
RT "The major facilitator transporter Str3 is required for low-affinity heme
RT acquisition in Schizosaccharomyces pombe.";
RL J. Biol. Chem. 293:6349-6362(2018).
CC -!- FUNCTION: High affinity heme transporter involved in the assimilation
CC of exogenous heme during conditions of low cellular iron.
CC {ECO:0000269|PubMed:25733668, ECO:0000269|PubMed:28193844,
CC ECO:0000269|PubMed:29549126}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:25733668,
CC ECO:0000269|PubMed:28193844}; Lipid-anchor, GPI-anchor
CC {ECO:0000305|PubMed:28193844}. Vacuole membrane
CC {ECO:0000269|PubMed:28193844}; Lipid-anchor, GPI-anchor
CC {ECO:0000305|PubMed:28193844}. Note=Localizes from the cell membrane to
CC the vacuolar membrane in the presence of heme.
CC {ECO:0000269|PubMed:28193844}.
CC -!- INDUCTION: Induced in iron-deplete conditions (at protein level)
CC (PubMed:25733668). Repressed in iron-replete conditions by
CC transcriptional repressor fep1 (PubMed:25733668).
CC {ECO:0000269|PubMed:25733668}.
CC -!- DISRUPTION PHENOTYPE: Impairs heme import into cell; simultaneous
CC disruption of str3 exacerbates the effect.
CC {ECO:0000269|PubMed:25733668, ECO:0000269|PubMed:28193844,
CC ECO:0000269|PubMed:29549126}.
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DR EMBL; CU329670; CAB03596.1; -; Genomic_DNA.
DR PIR; T38109; T38109.
DR RefSeq; NP_592791.1; NM_001018191.2.
DR AlphaFoldDB; Q92340; -.
DR BioGRID; 278312; 2.
DR STRING; 4896.SPAC1F8.02c.1; -.
DR PaxDb; Q92340; -.
DR EnsemblFungi; SPAC1F8.02c.1; SPAC1F8.02c.1:pep; SPAC1F8.02c.
DR GeneID; 2541821; -.
DR KEGG; spo:SPAC1F8.02c; -.
DR PomBase; SPAC1F8.02c; -.
DR VEuPathDB; FungiDB:SPAC1F8.02c; -.
DR HOGENOM; CLU_1225408_0_0_1; -.
DR PRO; PR:Q92340; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0031362; C:anchored component of external side of plasma membrane; TAS:PomBase.
DR GO; GO:0046658; C:anchored component of plasma membrane; IDA:PomBase.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:PomBase.
DR GO; GO:0000324; C:fungal-type vacuole; IDA:PomBase.
DR GO; GO:0005886; C:plasma membrane; IDA:PomBase.
DR GO; GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0020037; F:heme binding; IDA:PomBase.
DR GO; GO:0140488; F:heme receptor activity; IDA:PomBase.
DR GO; GO:0010106; P:cellular response to iron ion starvation; IMP:PomBase.
DR GO; GO:1904334; P:heme import across plasma membrane; IMP:PomBase.
DR GO; GO:0015886; P:heme transport; IMP:PomBase.
PE 1: Evidence at protein level;
KW Cell membrane; Glycoprotein; GPI-anchor; Lipoprotein; Membrane;
KW Reference proteome; Signal; Vacuole.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..199
FT /note="High affinity heme transporter"
FT /id="PRO_0000116632"
FT PROPEP 200..226
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000389138"
FT REGION 72..101
FT /note="Heme binding"
FT /evidence="ECO:0000269|PubMed:25733668"
FT LIPID 199
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000255"
FT MUTAGEN 72
FT /note="C->A: Decreases heme binding and cellular heme
FT import, and abolishes relocalization from the plasma
FT membrane to vacuole in presence of heme; when associated
FT with A-87; A-92 and A-101."
FT /evidence="ECO:0000269|PubMed:25733668,
FT ECO:0000269|PubMed:28193844"
FT MUTAGEN 87
FT /note="C->A: Decreases heme binding and cellular heme
FT import, and abolishes plasma membrane to vacuole
FT localization in presence of heme; when associated with A-
FT 72; A-92 and A-101."
FT /evidence="ECO:0000269|PubMed:25733668,
FT ECO:0000269|PubMed:28193844"
FT MUTAGEN 92
FT /note="C->A: Decreases heme binding and cellular heme
FT import, and abolishes plasma membrane to vacuole
FT localization in presence of heme; when associated with A-
FT 72; A-87 and A-101."
FT /evidence="ECO:0000269|PubMed:25733668,
FT ECO:0000269|PubMed:28193844"
FT MUTAGEN 101
FT /note="C->A: Decreases heme binding and cellular heme
FT import, and abolishes plasma membrane to vacuole
FT localization in presence of heme; when associated with A-
FT 72; A-87 and A-92."
FT /evidence="ECO:0000269|PubMed:25733668,
FT ECO:0000269|PubMed:28193844"
SQ SEQUENCE 226 AA; 25022 MW; 28E4AD7435525C00 CRC64;
MISLKIYFVL IFLFLKGINS AYVSNEEGET VDFTFSGFYA NLTYPNEISE LNYVEGNYLS
TRIVRFNGSF YCDTTILSET NNVTGSCYVA NCANDTVLEI CDSGKEVHFT DMSGTTWSAD
TFTENLYWFC GGDGNKPNMT TAAAMNSDID SYYVYGNWTI DTADSTVADY TCNYTHFQEA
GDIEKGDVYT ASADSSDSSS ASSTIFKPSY FISCLLSVGL YLVLNF
